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Literature summary for 2.6.1.1 extracted from
- Comparative studies on thermophilicity and thermostability of aspartate aminotransferases (1993), Biotechnol. Appl. Biochem., 18, 417-425.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate + 2-oxoglutarate | - |
Saccharolobus solfataricus | oxaloacetate + L-glutamate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AspAT | - |
Saccharolobus solfataricus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermophilicity, short-term and long-term thermostability of isoenzymes are independently evaluated and the influence of a cysteine residue on the three properties is assessed | Saccharolobus solfataricus |
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Release 2023.1 (January 2023)
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